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Journal of Bacteriology, February 2008, p. 1219-1223, Vol. 190, No. 4
0021-9193/08/$08.00+0     doi:10.1128/JB.01223-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Escherichia coli Cytosolic Glycerophosphodiester Phosphodiesterase (UgpQ) Requires Mg2+, Co2+, or Mn2+ for Its Enzyme Activity{triangledown}

Noriyasu Ohshima,* Saori Yamashita, Naoko Takahashi, Chizu Kuroishi, Yoshitsugu Shiro, and Koji Takio

RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan

Received 30 July 2007/ Accepted 30 November 2007

Escherichia coli cytosolic glycerophosphodiester phosphodiesterase, UgpQ, functions in the absence of other proteins encoded by the ugp operon and requires Mg2+, Mn2+, or Co2+, in contrast to Ca2+-dependent periplasmic glycerophosphodiester phosphodiesterase, GlpQ. UgpQ has broad substrate specificity toward various glycerophosphodiesters, producing sn-glycerol-3-phosphate and the corresponding alcohols. UgpQ accumulates under conditions of phosphate starvation, suggesting that it allows the utilization of glycerophosphodiesters as a source of phosphate. These results clarify how E. coli utilizes glycerophosphodiesters using two homologous enzymes, UgpQ and GlpQ.

* Corresponding author. Mailing address: RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan. Phone: 81-791-58-2553. Fax: 81-791-58-2522. E-mail: ohshima-tky{at}umin.ac.jp

{triangledown} Published ahead of print on 14 December 2007.

Journal of Bacteriology, February 2008, p. 1219-1223, Vol. 190, No. 4
0021-9193/08/$08.00+0     doi:10.1128/JB.01223-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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